R. Kaneko et N. Kitabatake, Sweetness of sweet protein thaumatin is more thermoresistant under acid conditions than under neutral or alkaline conditions, BIOS BIOT B, 65(2), 2001, pp. 409-413
Thermostability of thaumatin and mechanisms of thermoinactivation were exam
ined at 80 degreesC in the pH range from 2 to 10. The sweetness of thaumati
n disappeared on heating at pH above 7 for 15 min, but the sweetness remain
ed even after heating at 80 degreesC for 4 h at pH 2. This indicated that t
he sweet protein thaumatin is more thermoresistant under acid conditions th
an under neutral or alkaline conditions. Prolonged heating of thaumatin und
er acid conditions slowly reduced sweetness, and produced a heterogeneous p
opulation of molecules, all of which was soluble and monomeric. The resulta
nt molecules were clearly distinct from those generated by heating at pH ab
ove 7. Hydrolysis of peptide bonds and other irreversible chemical reaction
s slowly took place in the molecule heated under acid conditions, and it wo
uld be, in part, a cause of thermoinactivation of thaumatin under acid cond
itions. The thermostability of thaumatin and the mechanism of thermoinactiv
ation were largely dependent on pH.